메뉴 건너뛰기




Volumn 39, Issue 2, 1999, Pages 165-187

Detection and measurement of microbial lipase activity: A review

Author keywords

Bacteria; Esterases; Lipase substrates; Lipolytic activity; Microorganisms; Plate assay; Thermophilic

Indexed keywords

TRIACYLGLYCEROL LIPASE;

EID: 0033091456     PISSN: 10408398     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408399908500492     Document Type: Review
Times cited : (82)

References (96)
  • 1
    • 0001707489 scopus 로고
    • Heat resistant bacterial lipases and ultra-high temperature sterilization of dairy products
    • Adams, D. M. and Brawley, T. G. 1981. Heat resistant bacterial lipases and ultra-high temperature sterilization of dairy products. J. Dairy Sci. 64:1951-1957.
    • (1981) J. Dairy Sci. , vol.64 , pp. 1951-1957
    • Adams, D.M.1    Brawley, T.G.2
  • 2
    • 0015262781 scopus 로고
    • Rapid and sensitive assay for free fatty acids using rhodamine 6G
    • Anderson, M. M. and McCarty, R. E. 1972. Rapid and sensitive assay for free fatty acids using rhodamine 6G. Anal. Biochem. 45:260-270.
    • (1972) Anal. Biochem. , vol.45 , pp. 260-270
    • Anderson, M.M.1    McCarty, R.E.2
  • 3
    • 67349274048 scopus 로고
    • Association of Official Analytical Chemists, Inc., Arlington, VA
    • AOAC (Association of Official Analytical Chemists). 1990. Official Methods of Analysis. Fifteenth Edition. Association of Official Analytical Chemists, Inc., Arlington, VA.
    • (1990) Official Methods of Analysis. Fifteenth Edition
  • 4
    • 0024362958 scopus 로고
    • Rapid turbidimetric determination of lipase activity in biological fluids
    • Arzoglou, P. L., Tavridou, A., and Balaska, C. 1989. Rapid turbidimetric determination of lipase activity in biological fluids. Anal. Letters 226:1459-1469.
    • (1989) Anal. Letters , vol.226 , pp. 1459-1469
    • Arzoglou, P.L.1    Tavridou, A.2    Balaska, C.3
  • 5
    • 84883378772 scopus 로고
    • Conductimetric assay of a bacterial lipase, using triacetin as a substrate
    • Ballot, C., Favre-Bonvin, G., and Wallach, J. M. 1982. Conductimetric assay of a bacterial lipase, using triacetin as a substrate. Anal. Letters 15(B13):1119-1129.
    • (1982) Anal. Letters , vol.15 , Issue.B13 , pp. 1119-1129
    • Ballot, C.1    Favre-Bonvin, G.2    Wallach, J.M.3
  • 6
    • 0021752095 scopus 로고
    • Lipase assay in duodenal juice using a conductimetric method
    • Ballot, C., Favre-Bonvin, G., and Wallach, J. M. 1984. Lipase assay in duodenal juice using a conductimetric method. Clin. Chim. Acta 143:109-114.
    • (1984) Clin. Chim. Acta , vol.143 , pp. 109-114
    • Ballot, C.1    Favre-Bonvin, G.2    Wallach, J.M.3
  • 7
    • 0030824353 scopus 로고    scopus 로고
    • Determination of the kinetic parameters during continuous cultivation of the lipase-producing thermophile Bacillus sp. On olive oil
    • Becker, P., Abu-Reesh, I., Markossian, S., Antranikian, G., and Märkl, H. 1997. Determination of the kinetic parameters during continuous cultivation of the lipase-producing thermophile Bacillus sp. on olive oil. Appl. Microbiol. Biotechnol. 48:184-190.
    • (1997) Appl. Microbiol. Biotechnol. , vol.48 , pp. 184-190
    • Becker, P.1    Abu-Reesh, I.2    Markossian, S.3    Antranikian, G.4    Märkl, H.5
  • 8
    • 0030919230 scopus 로고    scopus 로고
    • Production and purification of a novel extracellular lipase from Alternaria brassicicola
    • Berto, P., Belingheri, L., and Dehorter, B. 1997. Production and purification of a novel extracellular lipase from Alternaria brassicicola. Biotechnol. Lett. 19:533-536.
    • (1997) Biotechnol. Lett. , vol.19 , pp. 533-536
    • Berto, P.1    Belingheri, L.2    Dehorter, B.3
  • 9
    • 0027956336 scopus 로고
    • Lipase production from an alkalophilic yeast species by solid state fermentation
    • Bhushan, B., Dosanjh, N. S., Kumar, K., and Hoondal, G. S. 1994. Lipase production from an alkalophilic yeast species by solid state fermentation. Biotechnol. Lett. 16:841-842.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 841-842
    • Bhushan, B.1    Dosanjh, N.S.2    Kumar, K.3    Hoondal, G.S.4
  • 10
    • 0021972169 scopus 로고
    • Quantitative studies of heat-stable proteinase from Pseudomonas fluorescens P1 by enzyme-linked immunosorbent assay
    • Birkeland, S-E., Stepaniak, L., and Sørhaug, T. 1985. Quantitative studies of heat-stable proteinase from Pseudomonas fluorescens P1 by enzyme-linked immunosorbent assay. Appl. Environ. Microbiol. 49: 382-387.
    • (1985) Appl. Environ. Microbiol. , vol.49 , pp. 382-387
    • Birkeland, S.-E.1    Stepaniak, L.2    Sørhaug, T.3
  • 12
    • 0019410913 scopus 로고
    • Colorimetric method for free fatty acids in serum validated by comparison with gas chromatography
    • Brunk, S.D. and Swanson, J.R. 1981. Colorimetric method for free fatty acids in serum validated by comparison with gas chromatography. Clin. Chem. 27:924-926.
    • (1981) Clin. Chem. , vol.27 , pp. 924-926
    • Brunk, S.D.1    Swanson, J.R.2
  • 13
    • 0030930428 scopus 로고    scopus 로고
    • Lipases in supercritical fluids
    • Cernia, E. and Palocci, C. 1997. Lipases in supercritical fluids. Methods Enzymol. 296 (B):495-508.
    • (1997) Methods Enzymol. , vol.296 , Issue.B , pp. 495-508
    • Cernia, E.1    Palocci, C.2
  • 14
    • 0039026977 scopus 로고
    • Gas chromatographic determination of free fatty acids in vegetable oils by a modified esterification procedure
    • Chapman, G. W., Jr. 1979. Gas Chromatographic determination of free fatty acids in vegetable oils by a modified esterification procedure. J. Am. Oil Chem. Soc. 56:77-79.
    • (1979) J. Am. Oil Chem. Soc. , vol.56 , pp. 77-79
    • Chapman G.W., Jr.1
  • 15
    • 0027771580 scopus 로고
    • Enhancement of lipase production during fed-batch cultivation of Pseudomonas aeruginosa MB 5001
    • Chartrain, M., Marcin, C., Katz, L., Salmon, P., Brix, T., Buckland, B., and Greasham, R. 1993. Enhancement of lipase production during fed-batch cultivation of Pseudomonas aeruginosa MB 5001. J. Ferm. Bioeng. 76:487-492.
    • (1993) J. Ferm. Bioeng. , vol.76 , pp. 487-492
    • Chartrain, M.1    Marcin, C.2    Katz, L.3    Salmon, P.4    Brix, T.5    Buckland, B.6    Greasham, R.7
  • 16
  • 17
    • 0025202709 scopus 로고
    • Reaction scheme of lipase production by Candida rugosa growing on olive oil
    • Del Rfo, J. L., Serra, P., Valero, F., Poch, M., and Solà, C. 1990. Reaction scheme of lipase production by Candida rugosa growing on olive oil. Biotechnol. Lett. 12:835-838.
    • (1990) Biotechnol. Lett. , vol.12 , pp. 835-838
    • Del Rfo, J.L.1    Serra, P.2    Valero, F.3    Poch, M.4    Solà, C.5
  • 18
    • 0027388770 scopus 로고
    • News from the interface: The molecular structures of triacylglyceride lipases
    • Derewenda, Z. S. and Sharp, A. M. 1993. News from the interface: the molecular structures of triacylglyceride lipases. Trends Biochem. Sci. 18:20-25.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 20-25
    • Derewenda, Z.S.1    Sharp, A.M.2
  • 20
    • 0017043559 scopus 로고
    • Some properties of the lipase of Geotrichum candidum evaluated by a fluorimetric assay technique
    • Dooijewaard-Kloosterziel, A. M. P. and Wouters, J. T. M. 1976. Some properties of the lipase of Geotrichum candidum evaluated by a fluorimetric assay technique. J. Appl. Bact. 40:293-299.
    • (1976) J. Appl. Bact. , vol.40 , pp. 293-299
    • Dooijewaard-Kloosterziel, A.M.P.1    Wouters, J.T.M.2
  • 21
    • 0002322351 scopus 로고
    • The colorimetric micro-determination of long-chain fatty acids
    • Duncombe, W. G. 1963. The colorimetric micro-determination of long-chain fatty acids. Biochem. J. 88:7-10.
    • (1963) Biochem. J. , vol.88 , pp. 7-10
    • Duncombe, W.G.1
  • 22
    • 0024532911 scopus 로고
    • Simple high performance liquid chromatography methods for monitoring lipase reactions
    • Ergan, F. and André, G. 1989. Simple high performance liquid chromatography methods for monitoring lipase reactions. Lipids 24:76-78.
    • (1989) Lipids , vol.24 , pp. 76-78
    • Ergan, F.1    André, G.2
  • 23
    • 0020713292 scopus 로고
    • Isolation and some properties of extracellular heat-stable lipases from Pseudomonas fluorescens strain AFT 36
    • Fox, P. F. and Stepaniak, L. 1983. Isolation and some properties of extracellular heat-stable lipases from Pseudomonas fluorescens strain AFT 36. J. Dairy Res. 50:77-89.
    • (1983) J. Dairy Res. , vol.50 , pp. 77-89
    • Fox, P.F.1    Stepaniak, L.2
  • 24
    • 0029186707 scopus 로고
    • Extracellular lipase production by a sapwood-staining fungus, Ophiostoma piceae
    • Gao, Y. and Breuil, C. 1995. Extracellular lipase production by a sapwood-staining fungus, Ophiostoma piceae. World J. Microbiol. Biotechnol. 11:638-642.
    • (1995) World J. Microbiol. Biotechnol. , vol.11 , pp. 638-642
    • Gao, Y.1    Breuil, C.2
  • 26
    • 0025809090 scopus 로고
    • Production of lipase by Yarrowia lipolytica. I. Lipases from yeasts
    • Hadeball, W. 1991. Production of lipase by Yarrowia lipolytica. I. Lipases from yeasts (Review). Acta Biotechnol. 11:159-167.
    • (1991) Acta Biotechnol. , vol.11 , pp. 159-167
    • Hadeball, W.1
  • 27
    • 84941842988 scopus 로고
    • Determination of α-amylase, trypsin and lipase in duodenal fluid: Comparison of methods
    • Hafkenscheid, J. C. M., Hessels, M., and van der Hoek, E. W. 1983. Determination of α-amylase, trypsin and lipase in duodenal fluid: comparison of methods. J. Clin. Chem. Clin. Biochem. 21:167-174.
    • (1983) J. Clin. Chem. Clin. Biochem. , vol.21 , pp. 167-174
    • Hafkenscheid, J.C.M.1    Hessels, M.2    Van Der Hoek, E.W.3
  • 28
    • 51249170526 scopus 로고
    • Screening of lipase activities with cultures from the agricultural research service culture collection
    • Hou, C. T. and Johnston, T. M. 1992. Screening of lipase activities with cultures from the Agricultural Research Service culture collection. J. Am. Oil Chem. Soc. 69:1088-1097.
    • (1992) J. Am. Oil Chem. Soc. , vol.69 , pp. 1088-1097
    • Hou, C.T.1    Johnston, T.M.2
  • 29
    • 0019429547 scopus 로고
    • A sensitive method for the determination of free fatty acids in plasma
    • Hron, W. T. and Menahan, L. A. 1981. A sensitive method for the determination of free fatty acids in plasma. J. Lipid Res. 22:377-381.
    • (1981) J. Lipid Res. , vol.22 , pp. 377-381
    • Hron, W.T.1    Menahan, L.A.2
  • 30
    • 0031212407 scopus 로고    scopus 로고
    • Enrichment of γ-linolenic acid from borage oil via lipase-catalyzed reactions
    • Huang, F-C., Ju, Y-H., and Huang, C-W. 1997. Enrichment of γ-linolenic acid from borage oil via lipase-catalyzed reactions. J. Am. Oil Chem. Soc. 74:977-981.
    • (1997) J. Am. Oil Chem. Soc. , vol.74 , pp. 977-981
    • Huang, F.-C.1    Ju, Y.-H.2    Huang, C.-W.3
  • 31
    • 0343457387 scopus 로고
    • Purification and characterization of a thermostable lipase from newly isolated Pseudomonas sp. KWI-56
    • Iizumi, T., Nakamura, K., and Fukase, T. 1990. Purification and characterization of a thermostable lipase from newly isolated Pseudomonas sp. KWI-56. Agric. Biol. Chem. 54:1253-1258.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 1253-1258
    • Iizumi, T.1    Nakamura, K.2    Fukase, T.3
  • 32
    • 0003107818 scopus 로고
    • Fungal lipase
    • Borgström, B. and Brockman, H. L., Eds., Elsevier Science Publishers, Amsterdam
    • Iwai, M. and Tsujisaka, Y. 1984. Fungal lipase. In: Lipases, pp. 443-469. Borgström, B. and Brockman, H. L., Eds., Elsevier Science Publishers, Amsterdam.
    • (1984) Lipases , pp. 443-469
    • Iwai, M.1    Tsujisaka, Y.2
  • 33
    • 0014150668 scopus 로고
    • Fluorometric assay for the hydrolytic activity of lipase using fatty acyl esters of 4-methylumbelliferone
    • Jacks, T. J. and Kircher, H. W. 1967. Fluorometric assay for the hydrolytic activity of lipase using fatty acyl esters of 4-methylumbelliferone. Anal. Biochem. 21: 279-285.
    • (1967) Anal. Biochem. , vol.21 , pp. 279-285
    • Jacks, T.J.1    Kircher, H.W.2
  • 34
    • 0029778830 scopus 로고    scopus 로고
    • Biotechnological application of Pseudomonas aeruginosa lipase: Efficient kinetic resolution of amines and alcohols
    • Jaeger, K-E., Liebeton, K., Zonta, A., Schimossek, K., and Reetz, M. T. 1996. Biotechnological application of Pseudomonas aeruginosa lipase: efficient kinetic resolution of amines and alcohols. Appl. Microbiol. Biotechnol. 46:99-105.
    • (1996) Appl. Microbiol. Biotechnol. , vol.46 , pp. 99-105
    • Jaeger, K.-E.1    Liebeton, K.2    Zonta, A.3    Schimossek, K.4    Reetz, M.T.5
  • 36
    • 0030847937 scopus 로고    scopus 로고
    • Qualitative rhodamine B assay which uses tallow as a substrate for lipolytic obligately anaerobic bacteria
    • Jarvis, G. N. and Thiele, J. H. 1997. Qualitative rhodamine B assay which uses tallow as a substrate for lipolytic obligately anaerobic bacteria. J. Microbiol. Methods 29:41-47.
    • (1997) J. Microbiol. Methods , vol.29 , pp. 41-47
    • Jarvis, G.N.1    Thiele, J.H.2
  • 37
    • 0021036393 scopus 로고
    • Detection and determination of lipase (acylglycerol hydrolase) activity from various sources
    • Jensen, R. B. 1983. Detection and determination of lipase (acylglycerol hydrolase) activity from various sources. Lipids 18:650-657.
    • (1983) Lipids , vol.18 , pp. 650-657
    • Jensen, R.B.1
  • 38
    • 0019196244 scopus 로고
    • A micromethod using gas-liquid chromatography for measuring individual fatty acids liberated during interaction of triglyceride-rich lipoproteins and lipoprotein lipase
    • Kashyap, M. L., Mellies, M. J., Brady, D., Hynd, B. A., and Robinson, K. 1980. A micromethod using gas-liquid chromatography for measuring individual fatty acids liberated during interaction of triglyceride-rich lipoproteins and lipoprotein lipase. Anal. Biochem. 107:432-435.
    • (1980) Anal. Biochem. , vol.107 , pp. 432-435
    • Kashyap, M.L.1    Mellies, M.J.2    Brady, D.3    Hynd, B.A.4    Robinson, K.5
  • 40
    • 85007967936 scopus 로고
    • Purification and characterization of an alkaline lipase from Pseudomonas fluorescens AK102
    • Kojima, Y., Yokoe, M., and Mase, T. 1994. Purification and characterization of an alkaline lipase from Pseudomonas fluorescens AK102. Biosci. Biotech. Biochem. 58:1564-1568.
    • (1994) Biosci. Biotech. Biochem. , vol.58 , pp. 1564-1568
    • Kojima, Y.1    Yokoe, M.2    Mase, T.3
  • 41
    • 0025914935 scopus 로고
    • Extracellular lipase of Pseudomonas sp. Strain ATCC 21808: Purification, characterization, crystallization, and preliminary X-ray diffraction data
    • Kordel, M., Hofmann, B., Schomburg, D., and Schmid, R. D. 1991. Extracellular lipase of Pseudomonas sp. strain ATCC 21808: purification, characterization, crystallization, and preliminary X-ray diffraction data. J. Bacteriol 173:4836-1841.
    • (1991) J. Bacteriol , vol.173 , pp. 4836-11841
    • Kordel, M.1    Hofmann, B.2    Schomburg, D.3    Schmid, R.D.4
  • 42
    • 0023089142 scopus 로고
    • Specific and sensitive plate assay for bacterial lipases
    • Kouker, G. and Jaeger, K-E. 1987. Specific and sensitive plate assay for bacterial lipases. Appl. Environ. Microbiol. 53:211-213.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 211-213
    • Kouker, G.1    Jaeger, K.-E.2
  • 46
    • 0015309472 scopus 로고
    • A rapid photometric micromethod for serum lipase determination
    • Lippi, U., Stevanato, G., and Guidi, G. 1972. A rapid photometric micromethod for serum lipase determination. Clin. Chim. Acta 37:199-202.
    • (1972) Clin. Chim. Acta , vol.37 , pp. 199-202
    • Lippi, U.1    Stevanato, G.2    Guidi, G.3
  • 47
    • 0030911253 scopus 로고    scopus 로고
    • Purification and characterization of lipase from Aeromonas sobria LP004
    • Lotrakul, P. and Dharmsthiti, S. 1997. Purification and characterization of lipase from Aeromonas sobria LP004. J. Biotechnol. 54:113-120.
    • (1997) J. Biotechnol. , vol.54 , pp. 113-120
    • Lotrakul, P.1    Dharmsthiti, S.2
  • 48
    • 0030570083 scopus 로고    scopus 로고
    • On the issue of interfacial activation of lipase in nonaqueous media
    • Louwrier, A., Drtina, G. J., and Klibanov, A. M. 1996. On the issue of interfacial activation of lipase in nonaqueous media. Biotechnol. Bioeng. 50:1-5.
    • (1996) Biotechnol. Bioeng. , vol.50 , pp. 1-5
    • Louwrier, A.1    Drtina, G.J.2    Klibanov, A.M.3
  • 49
    • 0016979036 scopus 로고
    • Rapid colorimetric determination of free fatty acids
    • Lowry, R. L. and Tinsley, I. J. 1976. Rapid colorimetric determination of free fatty acids. J. Am. Oil Chem. Soc. 53:470-472.
    • (1976) J. Am. Oil Chem. Soc. , vol.53 , pp. 470-472
    • Lowry, R.L.1    Tinsley, I.J.2
  • 50
    • 0001309793 scopus 로고
    • Engineering triacylglycerols. The role of interesterification
    • Marangoni, A. G. and Rousseau, D. 1995. Engineering triacylglycerols. The role of interesterification. Trends Food Sci. Technol. 6:329-335
    • (1995) Trends Food Sci. Technol. , vol.6 , pp. 329-335
    • Marangoni, A.G.1    Rousseau, D.2
  • 51
    • 0029965543 scopus 로고    scopus 로고
    • Some factors affecting lipase production by yeasts and filamentous fungi
    • Marek, A. and Bednarski, W. 1996. Some factors affecting lipase production by yeasts and filamentous fungi. Biotechnol. Lett. 18:1155-1160.
    • (1996) Biotechnol. Lett. , vol.18 , pp. 1155-1160
    • Marek, A.1    Bednarski, W.2
  • 52
    • 0030267827 scopus 로고    scopus 로고
    • Lipase production by lactic acid bacteria and activity on butter oil
    • Meyers, S. A., Cuppett, S. L., and Hutkins, R. W. 1996. Lipase production by lactic acid bacteria and activity on butter oil. Food Microbiol. 13:383-389.
    • (1996) Food Microbiol. , vol.13 , pp. 383-389
    • Meyers, S.A.1    Cuppett, S.L.2    Hutkins, R.W.3
  • 54
    • 51249176829 scopus 로고
    • Characteristics of an immobilized lipase for the commercial synthesis of esters
    • Miller, C., Austin, H., Posorske, L., and Gonzalez, J. 1988. Characteristics of an immobilized lipase for the commercial synthesis of esters. J. Am. Oil Chem. Soc. 68:927-931
    • (1988) J. Am. Oil Chem. Soc. , vol.68 , pp. 927-931
    • Miller, C.1    Austin, H.2    Posorske, L.3    Gonzalez, J.4
  • 55
    • 0019254034 scopus 로고
    • A new enzymatic method for colorimetric determination of free fatty acids
    • Mizuno, K., Toyosato, M., Yabumoto, S., Tanimizu, I., and Hirakawa, H. 1980. A new enzymatic method for colorimetric determination of free fatty acids. Anal. Biochem. 108:6-10.
    • (1980) Anal. Biochem. , vol.108 , pp. 6-10
    • Mizuno, K.1    Toyosato, M.2    Yabumoto, S.3    Tanimizu, I.4    Hirakawa, H.5
  • 56
    • 0027593821 scopus 로고
    • Rhizopus arrhizus lipase-catalyzed interesterification of the midfraction of palm oil to a cocoa butter equivalent fat
    • Mojovic, L., Siler-Marinkovic, S., Kukic, G., and Vunjak-Novakovic, G. 1993. Rhizopus arrhizus lipase-catalyzed interesterification of the midfraction of palm oil to a cocoa butter equivalent fat. Enzyme Microb. Technol. 15:438-443.
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 438-443
    • Mojovic, L.1    Siler-Marinkovic, S.2    Kukic, G.3    Vunjak-Novakovic, G.4
  • 61
    • 0001593186 scopus 로고
    • Lipids and related substances inducing the lipase production by Candida paralipolytica
    • Ota, Y., Suzuki, M., and Yamada, K. 1968. Lipids and related substances inducing the lipase production by Candida paralipolytica. Agric. Biol. Chem. 32:390-391.
    • (1968) Agric. Biol. Chem. , vol.32 , pp. 390-391
    • Ota, Y.1    Suzuki, M.2    Yamada, K.3
  • 63
    • 0002269446 scopus 로고    scopus 로고
    • Hydrolysis of milk fat by lipase in solvent-free phospholipid reverse micellar media
    • Patel, M. T., Nagarajan, R., and Kilara, A. 1996. Hydrolysis of milk fat by lipase in solvent-free phospholipid reverse micellar media. J. Food Sci. 61:33-38, 73.
    • (1996) J. Food Sci. , vol.61 , pp. 33-38
    • Patel, M.T.1    Nagarajan, R.2    Kilara, A.3
  • 64
    • 0019521379 scopus 로고
    • A new assay of microbial lipases with emulsified trioleoyl glycerol
    • Peled, N. and Krenz, M. C. 1981. A new assay of microbial lipases with emulsified trioleoyl glycerol. Anal. Biochem. 112:219-222.
    • (1981) Anal. Biochem. , vol.112 , pp. 219-222
    • Peled, N.1    Krenz, M.C.2
  • 65
    • 0030152430 scopus 로고    scopus 로고
    • Hydrolysis of p-nitrophenyl palmitate in n-heptane by the Pseudomonas cepacia lipase: A simple test for the determination of lipase activity in organic media
    • Pencreac'h, G. and Baratti, J. C. 1996. Hydrolysis of p-nitrophenyl palmitate in n-heptane by the Pseudomonas cepacia lipase: a simple test for the determination of lipase activity in organic media. Enz. Microb. Technol. 18:417-422.
    • (1996) Enz. Microb. Technol. , vol.18 , pp. 417-422
    • Pencreac'h, G.1    Baratti, J.C.2
  • 66
    • 26844479299 scopus 로고    scopus 로고
    • A stable lipase from Candida lipolytica. Cultivation conditions and crude enzyme characteristics
    • Pereira-Meirelles, F. V., Rocho-Leão, M. H. M., and Sant' Anna, G. L., Jr. 1997. A stable lipase from Candida lipolytica. Cultivation conditions and crude enzyme characteristics. Appl. Biochem. Biotechnol. 63-65:73-85.
    • (1997) Appl. Biochem. Biotechnol. , vol.63-65 , pp. 73-85
    • Pereira-Meirelles, F.V.1    Rocho-Leão, M.H.M.2    Sant' Anna G.L., Jr.3
  • 67
    • 0002309937 scopus 로고
    • Interesterification - Current status and future prospects
    • Przybylski, R. and McDonald, B. E., Eds., AOCS Press, Champaign, IL
    • Ramamurthi, S. and McCurdy, A. R. 1995. Interesterification - Current status and future prospects. In: Development and Processing of Vegetable Oils for Human Nutrition. pp. 62-68. Przybylski, R. and McDonald, B. E., Eds., AOCS Press, Champaign, IL.
    • (1995) Development and Processing of Vegetable Oils for Human Nutrition. , pp. 62-68
    • Ramamurthi, S.1    McCurdy, A.R.2
  • 68
    • 0024452172 scopus 로고
    • A single and continuous spectrophotometric assay for lipolytic enzymes, using natural, non-labelled lipid substrates
    • Rawyler, A. and Siegenthaler, P. A. 1989. A single and continuous spectrophotometric assay for lipolytic enzymes, using natural, non-labelled lipid substrates. Biochim. Biophys. Acta 1004:337-344.
    • (1989) Biochim. Biophys. Acta , vol.1004 , pp. 337-344
    • Rawyler, A.1    Siegenthaler, P.A.2
  • 71
    • 0001521210 scopus 로고
    • An inducible, intracellular, alkalophilic lipase in Aspergillus flavipes grown on triacylglycerols
    • Savitha, J. and Ratledge, C. 1992. An inducible, intracellular, alkalophilic lipase in Aspergillus flavipes grown on triacylglycerols. World J. Microbiol. Biotechnol. 8:129-131.
    • (1992) World J. Microbiol. Biotechnol. , vol.8 , pp. 129-131
    • Savitha, J.1    Ratledge, C.2
  • 72
    • 0031128209 scopus 로고    scopus 로고
    • Lipase-catalyzed synthesis of tricaprylin in a medium solely composed of substrates. Water production and elimination
    • Selmi, B., Gontier, E., Ergan, F., Barbotin, J, N., and Thomas, D. 1997. Lipase-catalyzed synthesis of tricaprylin in a medium solely composed of substrates. Water production and elimination. Enzyme Microb. Technol. 20:322-325.
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 322-325
    • Selmi, B.1    Gontier, E.2    Ergan, F.3    Barbotin, J.N.4    Thomas, D.5
  • 73
    • 0026565567 scopus 로고
    • Production, purification, and properties of a lipase from a bacterium (Pseudomonas aeruginosa YS-7) capable of growing in water-restricted environments
    • Shabtai, Y. and Daya-Mishne, N. 1992. Production, purification, and properties of a lipase from a bacterium (Pseudomonas aeruginosa YS-7) capable of growing in water-restricted environments. Appl. Environ. Microbiol. 58:174-180.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 174-180
    • Shabtai, Y.1    Daya-Mishne, N.2
  • 74
    • 0023144607 scopus 로고
    • Review of methods of enumeration, detection and isolation of lipolytic microorganisms with special reference to dairy applications
    • Shelley, A. W., Deeth, H. C., and MacRae, I. C. 1987. Review of methods of enumeration, detection and isolation of lipolytic microorganisms with special reference to dairy applications. J. Microbiol. Methods 6:123-137.
    • (1987) J. Microbiol. Methods , vol.6 , pp. 123-137
    • Shelley, A.W.1    Deeth, H.C.2    MacRae, I.C.3
  • 75
    • 0029921719 scopus 로고    scopus 로고
    • Characteristics and kinetics of lipase-catalyzed hydrolysis of olive oil in a reverse micellar system
    • Shiomori, K., Ishimura, M., Baba, Y., Kawano, Y., Kuboi, R., and Komasawa, I. 1996. Characteristics and kinetics of lipase-catalyzed hydrolysis of olive oil in a reverse micellar system. J. Ferment. Bioeng. 81: 143-147.
    • (1996) J. Ferment. Bioeng. , vol.81 , pp. 143-147
    • Shiomori, K.1    Ishimura, M.2    Baba, Y.3    Kawano, Y.4    Kuboi, R.5    Komasawa, I.6
  • 76
    • 0026758994 scopus 로고
    • Induction of Geotrichum candidum lipase by long-chain fatty acids
    • Shimada, Y., Sugihara, A., Nagao, T., and Tominaga, Y. 1992. Induction of Geotrichum candidum lipase by long-chain fatty acids. J. Ferment. Bioeng. 74: 77-80.
    • (1992) J. Ferment. Bioeng. , vol.74 , pp. 77-80
    • Shimada, Y.1    Sugihara, A.2    Nagao, T.3    Tominaga, Y.4
  • 78
    • 0026758653 scopus 로고
    • Quantitative spectrophotometric assay for staphylococcal lipase
    • Smeltzer, M. S., Hart, M. E., and Iandolo, J. J. 1992. Quantitative spectrophotometric assay for staphylococcal lipase. Appl. Environ. Microbiol. 58:2815-2819.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2815-2819
    • Smeltzer, M.S.1    Hart, M.E.2    Iandolo, J.J.3
  • 79
    • 0004023636 scopus 로고
    • Lipolytic microorganisms
    • Vanderzant, C. and Splittstoesser, D. F., Eds., American Public Health Association, Washington, D.C.
    • Smith, J. L. and Haas, M. J. 1992. Lipolytic microorganisms. In: Compendium of Methods for the Microbiological Examination of Foods. pp. 183-191. Vanderzant, C. and Splittstoesser, D. F., Eds., American Public Health Association, Washington, D.C.
    • (1992) Compendium of Methods for the Microbiological Examination of Foods. , pp. 183-191
    • Smith, J.L.1    Haas, M.J.2
  • 80
    • 0025800683 scopus 로고
    • Evaluation of lipase selectivity of hydrolysis
    • Sonnet, P. E. and Gazzillo, J. A. 1991. Evaluation of lipase selectivity of hydrolysis. J. Am. Oil Chem. Soc. 68:11-15.
    • (1991) J. Am. Oil Chem. Soc. , vol.68 , pp. 11-15
    • Sonnet, P.E.1    Gazzillo, J.A.2
  • 81
    • 0022761182 scopus 로고
    • Microbial lipases: Their characteristics, role in food spoilage and industrial uses
    • Stead, D. 1986. Microbial lipases: their characteristics, role in food spoilage and industrial uses. J. Dairy Res. 53:481-505.
    • (1986) J. Dairy Res. , vol.53 , pp. 481-505
    • Stead, D.1
  • 82
    • 0024804348 scopus 로고
    • The effect of culture conditions on lipolytic productivity of Penicillium citrinum
    • Sztajer, H. and Maliszewska, I. 1989. The effect of culture conditions on lipolytic productivity of Penicillium citrinum. Biotechnol. Lett. 11:895-898.
    • (1989) Biotechnol. Lett. , vol.11 , pp. 895-898
    • Sztajer, H.1    Maliszewska, I.2
  • 83
    • 84987421546 scopus 로고
    • Microbial lipases in biotechnology
    • Sztajer, H. and Zboínska, E. 1988. Microbial lipases in biotechnology. Acta Biotechnol. 8:169-175.
    • (1988) Acta Biotechnol. , vol.8 , pp. 169-175
    • Sztajer, H.1    Zboínska, E.2
  • 84
    • 84986467066 scopus 로고
    • Variation in enzyme-linked immunosorbent assay (ELISA) components to lower sulfathiazole detection limits
    • Thomson, C. A. and Sporns, P. 1995. Variation in enzyme-linked immunosorbent assay (ELISA) components to lower sulfathiazole detection limits. J. Food Sci. 60:872-879.
    • (1995) J. Food Sci. , vol.60 , pp. 872-879
    • Thomson, C.A.1    Sporns, P.2
  • 85
    • 0019828930 scopus 로고
    • A rapid, simple and sensitive procedure for the determination of free fatty acids in plasma using glass capillary column gas-liquid chromatography
    • Tserng, K-Y., Kliegman, R. M., Miettinen, E-L., and Kalhan, S. C. 1981. A rapid, simple and sensitive procedure for the determination of free fatty acids in plasma using glass capillary column gas-liquid chromatography. J. Lipid Res. 22:852-858.
    • (1981) J. Lipid Res. , vol.22 , pp. 852-858
    • Tserng, K.-Y.1    Kliegman, R.M.2    Miettinen, E.-L.3    Kalhan, S.C.4
  • 86
    • 0000227583 scopus 로고    scopus 로고
    • Superinducers for induction of thermostable lipase production by Pseudomonas species NT-163 and other Pseudomonas-like bacteria
    • Ushio, K. Hirata, T., Yoshida, K., Sakaue, M., Hirose, C., Suzuki, T., and Ishizuka, M. 1996. Superinducers for induction of thermostable lipase production by Pseudomonas species NT-163 and other Pseudomonas-like bacteria. Biotechnol. Lett. 10:267-272.
    • (1996) Biotechnol. Lett. , vol.10 , pp. 267-272
    • Ushio, K.1    Hirata, T.2    Yoshida, K.3    Sakaue, M.4    Hirose, C.5    Suzuki, T.6    Ishizuka, M.7
  • 87
    • 0025306520 scopus 로고
    • A simple and sensitive method for the estimation of microbial lipase activity
    • Veeraragavan, K. 1990. A simple and sensitive method for the estimation of microbial lipase activity. Anal. Biochem. 186:301-305.
    • (1990) Anal. Biochem. , vol.186 , pp. 301-305
    • Veeraragavan, K.1
  • 88
    • 0018890516 scopus 로고
    • Enzyme kinetics of lipolysis
    • Verger, R. 1980. Enzyme kinetics of lipolysis. Methods Enzymol. 64:340-392.
    • (1980) Methods Enzymol. , vol.64 , pp. 340-392
    • Verger, R.1
  • 89
    • 0031023666 scopus 로고    scopus 로고
    • 'Interfacial activation' of lipases: Facts and artifacts
    • Verger, R. 1997. 'Interfacial activation' of lipases: facts and artifacts. TIBTECH 15:32-38.
    • (1997) TIBTECH , vol.15 , pp. 32-38
    • Verger, R.1
  • 90
    • 0009210076 scopus 로고
    • Background rejection in fluorescence immunoassay
    • Knapp, W., Holubar, K., and Wick, G., Eds., Elsevier/North Holland Biomedical Press, New York
    • Weider, I. 1978. Background rejection in fluorescence immunoassay. In: Immunofluorescence and Related Staining Techniques. pp. 67-80. Knapp, W., Holubar, K., and Wick, G., Eds., Elsevier/North Holland Biomedical Press, New York.
    • (1978) Immunofluorescence and Related Staining Techniques , pp. 67-80
    • Weider, I.1
  • 91
    • 0025355187 scopus 로고
    • A continuous fluorescence displacement assay for the measurement of phospholipase A2 and other lipases that release long-chain fatty acids
    • Wilton, D. C. 1990. A continuous fluorescence displacement assay for the measurement of phospholipase A2 and other lipases that release long-chain fatty acids. Biochem. J. 266:435-439.
    • (1990) Biochem. J. , vol.266 , pp. 435-439
    • Wilton, D.C.1
  • 92
    • 0025911613 scopus 로고
    • A continuous fluorescence-displacement assay for triacylglycerol lipase and phospholipase C that also allows the measurement of acylglycerols
    • Wilton, D. C. 1991. A continuous fluorescence-displacement assay for triacylglycerol lipase and phospholipase C that also allows the measurement of acylglycerols. Biochem. J. 276:129-133.
    • (1991) Biochem. J. , vol.276 , pp. 129-133
    • Wilton, D.C.1
  • 93
    • 0018399632 scopus 로고
    • Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens
    • Winkler, U. K. and Stuckmann, M. 1979. Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. J. Bacteriol. 138:663-670.
    • (1979) J. Bacteriol. , vol.138 , pp. 663-670
    • Winkler, U.K.1    Stuckmann, M.2
  • 94
    • 0026631279 scopus 로고
    • Water-soluble, dye-labelled fatty acid derivatives for preliminary detection of lipolytic microorganisms in agar media
    • Wirth, S. J. 1992. Water-soluble, dye-labelled fatty acid derivatives for preliminary detection of lipolytic microorganisms in agar media. FEMS Microbiol. Lett. 95:77-80.
    • (1992) FEMS Microbiol. Lett. , vol.95 , pp. 77-80
    • Wirth, S.J.1
  • 95
    • 0001478553 scopus 로고    scopus 로고
    • Kinetic studies on immobilised lipase esterification of oleic acid and octanol
    • Yong, Y. P. and Al-Duri, B. 1996. Kinetic studies on immobilised lipase esterification of oleic acid and octanol. J. Chem. Technol. Biotechnol. 65:239-248.
    • (1996) J. Chem. Technol. Biotechnol. , vol.65 , pp. 239-248
    • Yong, Y.P.1    Al-Duri, B.2
  • 96
    • 0024278258 scopus 로고
    • Enzyme catalysis in nonaqueous solvents
    • Zaks, A. and Klibanov, A. M. 1988. Enzyme catalysis in nonaqueous solvents. J. Biol. Chem. 263:3194-3201.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.